Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process
Prolyl <i>cis</i>/<i>trans</i> isomerization is a rate-limiting step in protein folding, often coupling directly to the acquisition of native structure. Here, we investigated the interplay between folding and prolyl isomerization in the N2 domain of the gene-3-protein from fi...
Saved in:
| Main Authors: | Ulrich Weininger, Maximilian von Delbrück, Franz X. Schmid, Roman P. Jakob |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-02-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/15/2/259 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Left $\phi$-biflatness and $\phi$-biprojectivity of certain Banach algebras with applications
by: Solaleh Salimi, et al.
Published: (2025-07-01) -
Conformational ensembles for protein structure prediction
by: Jiaan Yang, et al.
Published: (2025-03-01) -
Aluminum oxide carrier for a catalyst for low-temperature isomerization of hydrocarbons
by: N. Tagandurdyyeva, et al.
Published: (2020-07-01) -
Probing nanoparticle proximity effects on selective butadiene hydrogenation over Pd-Au/TiO2 with parahydrogen-induced polarization NMR
by: Bintian Lu, et al.
Published: (2025-06-01) -
Expose flexible conformations for intrinsically disordered protein
by: Jiaan Yang, et al.
Published: (2025-12-01)